ID   UMPS_ARATH              Reviewed;         476 AA.
AC   Q42586; Q9M1I0;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   06-JUN-2002, sequence version 2.
DT   24-JAN-2024, entry version 156.
DE   RecName: Full=Uridine 5'-monophosphate synthase;
DE            Short=UMP synthase;
DE   Includes:
DE     RecName: Full=Orotate phosphoribosyltransferase;
DE              Short=OPRTase;
DE              EC=2.4.2.10;
DE   Includes:
DE     RecName: Full=Orotidine 5'-phosphate decarboxylase;
DE              EC=4.1.1.23;
DE     AltName: Full=OMPdecase;
GN   Name=PYRE-F; Synonyms=UMPS; OrderedLocusNames=At3g54470;
GN   ORFNames=T14E10.40;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8041358; DOI=10.1007/bf00280183;
RA   Nasr F., Bertauche N., Dufour M.E., Minet M., Lacroute F.;
RT   "Heterospecific cloning of Arabidopsis thaliana cDNAs by direct
RT   complementation of pyrimidine auxotrophic mutants of Saccharomyces
RT   cerevisiae. I. Cloning and sequence analysis of two cDNAs catalysing the
RT   second, fifth and sixth steps of the de novo pyrimidine biosynthesis
RT   pathway.";
RL   Mol. Gen. Genet. 244:23-32(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. Columbia;
RA   Kafer C.W., Thornburg R.W.;
RT   "Transcriptional analysis of the Arabidopsis thaliana UMP synthase locus.";
RL   Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(2000).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-
CC         ribose 1-diphosphate + orotate; Xref=Rhea:RHEA:10380,
CC         ChEBI:CHEBI:30839, ChEBI:CHEBI:33019, ChEBI:CHEBI:57538,
CC         ChEBI:CHEBI:58017; EC=2.4.2.10;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + orotidine 5'-phosphate = CO2 + UMP;
CC         Xref=Rhea:RHEA:11596, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57538, ChEBI:CHEBI:57865; EC=4.1.1.23;
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       UMP from orotate: step 1/2.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       UMP from orotate: step 2/2.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the purine/pyrimidine
CC       phosphoribosyltransferase family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the OMP decarboxylase
CC       family. {ECO:0000305}.
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DR   EMBL; X71842; CAA50686.1; -; mRNA.
DR   EMBL; AF276887; AAK69440.1; -; Genomic_DNA.
DR   EMBL; AL138656; CAB77567.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE79235.1; -; Genomic_DNA.
DR   EMBL; AY140098; AAM98239.1; -; mRNA.
DR   EMBL; BT006612; AAP31956.1; -; mRNA.
DR   PIR; S46440; S46440.
DR   PIR; T47606; T47606.
DR   RefSeq; NP_680130.1; NM_148875.5.
DR   AlphaFoldDB; Q42586; -.
DR   SMR; Q42586; -.
DR   BioGRID; 9928; 3.
DR   IntAct; Q42586; 1.
DR   STRING; 3702.Q42586; -.
DR   PaxDb; 3702-AT3G54470-1; -.
DR   ProteomicsDB; 245270; -.
DR   EnsemblPlants; AT3G54470.1; AT3G54470.1; AT3G54470.
DR   GeneID; 824612; -.
DR   Gramene; AT3G54470.1; AT3G54470.1; AT3G54470.
DR   KEGG; ath:AT3G54470; -.
DR   Araport; AT3G54470; -.
DR   TAIR; AT3G54470; -.
DR   eggNOG; KOG1377; Eukaryota.
DR   HOGENOM; CLU_049275_1_0_1; -.
DR   InParanoid; Q42586; -.
DR   OMA; SAKHVCG; -.
DR   OrthoDB; 922at2759; -.
DR   PhylomeDB; Q42586; -.
DR   BioCyc; ARA:AT3G54470-MONOMER; -.
DR   BioCyc; MetaCyc:AT3G54470-MONOMER; -.
DR   UniPathway; UPA00070; UER00119.
DR   UniPathway; UPA00070; UER00120.
DR   PRO; PR:Q42586; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q42586; baseline and differential.
DR   GO; GO:0004588; F:orotate phosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR   GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016036; P:cellular response to phosphate starvation; IEP:TAIR.
DR   CDD; cd04725; OMP_decarboxylase_like; 1.
DR   CDD; cd06223; PRTases_typeI; 1.
DR   Gene3D; 3.40.50.2020; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   HAMAP; MF_01208; PyrE; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR014732; OMPdecase.
DR   InterPro; IPR018089; OMPdecase_AS.
DR   InterPro; IPR001754; OMPdeCOase_dom.
DR   InterPro; IPR023031; OPRT.
DR   InterPro; IPR004467; Or_phspho_trans_dom.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR029057; PRTase-like.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   NCBIfam; TIGR00336; pyrE; 1.
DR   NCBIfam; TIGR01740; pyrF; 1.
DR   PANTHER; PTHR19278; OROTATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR19278:SF9; URIDINE 5'-MONOPHOSPHATE SYNTHASE; 1.
DR   Pfam; PF00215; OMPdecase; 1.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   SMART; SM00934; OMPdecase; 1.
DR   SUPFAM; SSF53271; PRTase-like; 1.
DR   SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
DR   PROSITE; PS00156; OMPDECASE; 1.
DR   PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
PE   2: Evidence at transcript level;
KW   Decarboxylase; Glycosyltransferase; Lyase; Multifunctional enzyme;
KW   Pyrimidine biosynthesis; Reference proteome; Transferase.
FT   CHAIN           1..476
FT                   /note="Uridine 5'-monophosphate synthase"
FT                   /id="PRO_0000139653"
FT   ACT_SITE        305
FT                   /evidence="ECO:0000250"
FT   CONFLICT        186
FT                   /note="V -> E (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   476 AA;  51850 MW;  F79AE7992503D928 CRC64;
     MSAMEALILQ LHEIGAVKFG NFKLKSGIFS PVYIDLRLIV SYPSLLTQIS QTLISSLPPS
     ATFDVVCGVP YTALPIATVV SVSNGIPMLM RRKEIKDYGT SKAIEGIFEK DQTCLIIEDL
     VTSGASVLET AAPLRAVGLK VSDAVVLIDR QQGGRENLAE NGIKLHSMIM LTDMVRVLKE
     KGKIEVEVEV NLLKFLEENR RVSVPSVEKP KPKPRVLGFK ERSELSKNPT GKKLFDIMLK
     KETNLCLAAD VGTAAELLDI ADKVGPEICL LKTHVDILPD FTPDFGSKLR AIADKHKFLI
     FEDRKFADIG NTVTMQYEGG IFKILEWADI INAHVISGPG IVDGLKLKGM PRGRGLLLLA
     EMSSAGNLAT GDYTAAAVKI ADAHSDFVMG FISVNPASWK CGYVYPSMIH ATPGVQMVKG
     GDALGQQYNT PHSVITERGS DIIIVGRGII KAENPAETAH EYRVQGWNAY LEKCSQ
//